Guo Zhihao, Li Weiyu, Xue Yuan, Bo Liying, Ren Jian, Song Chunli
College of Food and Bioengineering, Qiqihar University, Qiqihar 161006, China.
School of Educational Science, Jiamusi University, Jiamusi 154007, China.
Foods. 2025 Apr 14;14(8):1353. doi: 10.3390/foods14081353.
Partially substituting other proteins in soy-protein-based products is an effective method to meet nutritional and application requirements. However, the emulsifying properties of soybean protein isolates (SPI) when partially substituted with zein hydrolysates (ZH) remain unknown. In the present work, protein blend (0 h-SPI/ZH) from SPI and ZH with a ratio of 3.5: 1 (/) was treated by transglutaminase (TGase) for 0, 0.5, 1.0, and 1.5 h, respectively. SDS-PAGE analysis results indicate protein polymers were generated in SPI/ZH conjugates. Emulsifying activity of the conjugates (1.5 h-SPI/ZH) was significantly increased from 23.69 to 28.13 m g in comparison with SPI, and there was no statistically significant difference ( < 0.05) in emulsion stability. The apparent viscosity, surface hydrophobicity of the SPI/ZH conjugates were significantly increased. Emulsion droplet size and zeta potential stabilized by 1.5 h-SPI/ZH were also increased; the values were 64.73 to 80.79 r.nm and -21.8 to -29.9 mV, respectively. CLSM results indicate that 1.5 h-SPI/ZH conjugates stabilized the emulsion and had a thicker adsorption layer. Overall, high values of negative zeta potential and suitable molecular weight distribution of the SPI/ZH conjugates might be responsible for the improved emulsifying property. This study provides insights for the preparation of soy-protein-based products as a promising food emulsifier.
在大豆蛋白基产品中部分替代其他蛋白质是满足营养和应用需求的有效方法。然而,用玉米醇溶蛋白水解物(ZH)部分替代大豆分离蛋白(SPI)时其乳化特性仍不清楚。在本研究中,将SPI与ZH比例为3.5:1(/)的蛋白混合物(0 h-SPI/ZH)分别用转谷氨酰胺酶(TGase)处理0、0.5、1.0和1.5小时。SDS-PAGE分析结果表明SPI/ZH共轭物中产生了蛋白质聚合物。与SPI相比,共轭物(1.5 h-SPI/ZH)的乳化活性从23.69显著提高到28.13 m g,且乳液稳定性无统计学显著差异(<0.05)。SPI/ZH共轭物的表观粘度、表面疏水性显著增加。由1.5 h-SPI/ZH稳定的乳液滴尺寸和zeta电位也增加;其值分别为64.73至80.79 r.nm和-21.8至-29.9 mV。CLSM结果表明1.5 h-SPI/ZH共轭物使乳液稳定且具有更厚的吸附层。总体而言,SPI/ZH共轭物的高负zeta电位值和合适的分子量分布可能是其乳化性能改善的原因。本研究为制备作为有前景的食品乳化剂的大豆蛋白基产品提供了见解。